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Volumn 323, Issue 1, 2004, Pages 24-31

Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A 2 in the monomeric and dimeric states: Insights into its oligomeric state

Author keywords

Acidic phospholipase A 2; Bothrops jararacussu venom; Crystal structure; Dimeric phospholipase A 2; Oligomeric state; Platelet aggregation and hypotensive effects; X ray crystallography

Indexed keywords

ANTIHYPERTENSIVE AGENT; ANTITHROMBOCYTIC AGENT; CALCIUM BINDING PROTEIN; DIMER; MONOMER; OLIGOMER; PHOSPHOLIPASE A2; SNAKE VENOM; SODIUM ION; CALCIUM ION;

EID: 4444265324     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.046     Document Type: Article
Times cited : (31)

References (49)
  • 2
    • 0010282916 scopus 로고
    • W. Shier D. Mebs Marcel Dekker New York
    • P. Rosenberg W. Shier D. Mebs Handbook of Toxinology 1990 Marcel Dekker New York 67 277
    • (1990) Handbook of Toxinology , pp. 67-277
    • Rosenberg, P.1
  • 4
    • 0031806039 scopus 로고    scopus 로고
    • Structure, function and biophysical aspects of the myotoxins from snake venoms
    • C.L. Ownby Structure, function and biophysical aspects of the myotoxins from snake venoms J. Toxicol. Toxin Rev. 17 1998 1003 1009
    • (1998) J. Toxicol. Toxin Rev. , vol.17 , pp. 1003-1009
    • Ownby, C.L.1
  • 7
    • 1042287118 scopus 로고    scopus 로고
    • 2 from snake venoms: Effects on catalytic and pharmacological properties. Review
    • 2 from snake venoms: effects on catalytic and pharmacological properties. Review Toxicon 42 2004 855 868
    • (2004) Toxicon , vol.42 , pp. 855-868
    • Soares, A.M.1    Giglio, J.R.2
  • 13
    • 4444225227 scopus 로고    scopus 로고
    • 2 myotoxins from Bothrops snake venoms: Structure-function relationship
    • in press
    • 2 myotoxins from Bothrops snake venoms: structure-function relationship, Curr. Org. Chem. 8 (2004) in press
    • (2004) Curr. Org. Chem. , vol.8
    • Soares, A.M.1    Fontes, M.R.2    Giglio, J.R.3
  • 17
    • 0033563920 scopus 로고    scopus 로고
    • Crystal structure of myotoxin II, a monomeric Lys49-phospholipase homologue isolated from the venom of Cerrophidion (Bothrops) godmani
    • R.K. Arni, M.R.M. Fontes, C. Barberato, J.M. Gutiérrez, C. Dí-az-Oreiro, and R.J. Ward Crystal structure of myotoxin II, a monomeric Lys49-phospholipase homologue isolated from the venom of Cerrophidion (Bothrops) godmani Arch. Biochem. Biophys. 366 1999 177 182
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 177-182
    • Arni, R.K.1    Fontes, M.R.M.2    Barberato, C.3    Gutiérrez, J.M.4    Dí-az-Oreiro, C.5    Ward, R.J.6
  • 19
    • 0037319939 scopus 로고    scopus 로고
    • 2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: Possible relationship to cooperative substrate binding
    • 2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: possible relationship to cooperative substrate binding Acta Crystallogr. D 59 2003 255 262
    • (2003) Acta Crystallogr. D , vol.59 , pp. 255-262
    • Rigden, D.J.1    Hwa, L.W.2    Marangoni, S.3    Toyama, M.H.4    Polikarpov, I.5
  • 21
    • 0033167306 scopus 로고    scopus 로고
    • A novel phospholipase A2, BJ-PLA2, from the venom of the snake Bothrops jararaca: Purification, primary structure analysis, and its characterization as a platelet-aggregation-inhibiting factor
    • S.M.T. Serrano, A.P. Reichl, R. Mentele, E.A. Auerswald, M.L. Santoro, C.A.M. Sampaio, A.C.M. Camargo, and M.T. Assakura A novel phospholipase A2, BJ-PLA2, from the venom of the snake Bothrops jararaca: purification, primary structure analysis, and its characterization as a platelet-aggregation- inhibiting factor Arch. Biochem. Biophys. 367 1999 26 32
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 26-32
    • Serrano, S.M.T.1    Reichl, A.P.2    Mentele, R.3    Auerswald, E.A.4    Santoro, M.L.5    Sampaio, C.A.M.6    Camargo, A.C.M.7    Assakura, M.T.8
  • 22
    • 0023878851 scopus 로고
    • Fractionation of Bothrops jararacussu snake venom: Partial chemical characterization and biological activity of bothropstoxin
    • M.I. Homsi-Brandeburgo, L.S. Queiroz, H. Santo-Neto, L. Rodrigues-Simioni, and J.R. Giglio Fractionation of Bothrops jararacussu snake venom: partial chemical characterization and biological activity of bothropstoxin Toxicon 26 1988 615 627
    • (1988) Toxicon , vol.26 , pp. 615-627
    • Homsi-Brandeburgo, M.I.1    Queiroz, L.S.2    Santo-Neto, H.3    Rodrigues-Simioni, L.4    Giglio, J.R.5
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallogr. A50 1994 157 163
    • (1994) Acta Crystallogr. , vol.50 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0031024454 scopus 로고    scopus 로고
    • Structural aspects of interfacial adsorption. a crystallographic and site-directed mutagenesis study of the phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus
    • S.K. Han, E.T. Yoon, D.L. Scott, P.B. Sigler, and W. Cho Structural aspects of interfacial adsorption. A crystallographic and site-directed mutagenesis study of the phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus J. Biol. Chem. 272 1997 3573 3582
    • (1997) J. Biol. Chem. , vol.272 , pp. 3573-3582
    • Han, S.K.1    Yoon, E.T.2    Scott, D.L.3    Sigler, P.B.4    Cho, W.5
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project No. 4 (CCP4), The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 39
    • 0036006762 scopus 로고    scopus 로고
    • Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus
    • L. Gu, H. Zhang, S. Song, Y. Zhou, and Z. Lin Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus Acta Crystallogr. D 58 2002 104 110
    • (2002) Acta Crystallogr. D , vol.58 , pp. 104-110
    • Gu, L.1    Zhang, H.2    Song, S.3    Zhou, Y.4    Lin, Z.5
  • 40
    • 0021827807 scopus 로고
    • The refined crystal structure of dimeric phospholipase A2 at 2.5 Å. Access to a shielded catalytic center
    • S. Brunie, J. Bolin, D. Gewirth, and P.B. Sigler The refined crystal structure of dimeric phospholipase A2 at 2.5 Å. Access to a shielded catalytic center J. Biol. Chem. 260 1985 9742 9749
    • (1985) J. Biol. Chem. , vol.260 , pp. 9742-9749
    • Brunie, S.1    Bolin, J.2    Gewirth, D.3    Sigler, P.B.4
  • 41
    • 0035207975 scopus 로고    scopus 로고
    • Regulation of catalytic function by molecular association: Structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 Å resolution
    • V. Chandra, P. Kaur, J. Jasti, C. Betzel, and T.P. Singh Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 Å resolution Acta Crystallogr. D 57 2001 1793 1798
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1793-1798
    • Chandra, V.1    Kaur, P.2    Jasti, J.3    Betzel, C.4    Singh, T.P.5
  • 42
    • 0032128325 scopus 로고    scopus 로고
    • Structure of a basic phospholipase A2 from Agkistrodon halys Pallas at 2.13 Å resolution
    • K. Zhao, S. Song, Z. Lin, and Y. Zhou Structure of a basic phospholipase A2 from Agkistrodon halys Pallas at 2.13 Å resolution Acta Crystallogr. D 510 1998 510 521
    • (1998) Acta Crystallogr. D , vol.510 , pp. 510-521
    • Zhao, K.1    Song, S.2    Lin, Z.3    Zhou, Y.4
  • 45
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • W.R. Pearson Rapid and sensitive sequence comparison with FASTP and FASTA Methods Enzymol. 183 1990 63 98
    • (1990) Methods Enzymol. , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 47
    • 0033951375 scopus 로고    scopus 로고
    • Outer-membrane phospholipase A: Known structure, unknown biological function
    • N. Dekker Outer-membrane phospholipase A: known structure, unknown biological function Mol. Microbiol. 35 2000 711 717
    • (2000) Mol. Microbiol. , vol.35 , pp. 711-717
    • Dekker, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.